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(S)-aminoethylcysteine + O2
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Substrates: monooxygenase activity
Products: -
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4-chlorolysine + O2
?
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Substrates: oxidase activity
Products: -
?
4-methyllysine + O2
2-keto-4-methyl-6-amino-n-hexanoate + NH3 + H2O2
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Substrates: oxidase activity
Products: -
?
5-hydroxylysine + O2
?
-
Substrates: oxidase activity
Products: -
?
5-methyllysine + O2
4-methyl-5-aminopentanamide + CO2 + H2O
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Substrates: monooxygenase activity
Products: -
?
alanine + propylamine + O2
?
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Substrates: monooxygenase and oxidase activity
Products: -
?
alanine + propylamine + phenazine methosulfate
pyruvate + NH3 + reduced phenazine methosulfate
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Substrates: anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
Products: -
?
DL-2,7-diaminoheptanoate + O2
?
-
Substrates: -
Products: -
r
DL-2,8-diaminooctanoate + O2
2-keto-8-aminooctanoate + NH3 + H2O2
-
Substrates: oxidase activity
Products: -
?
DL-5-hydroxylysine + O2
?
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Substrates: monooxygenase activity
Products: -
?
DL-7,8-diaminoheptanoate + O2
6-aminohexanamide + CO2 + H2O
-
Substrates: monooxygenase activity
Products: -
?
L-arginine + O2
2-amino-5-guanidinovalerate + NH3 + H2O2
-
Substrates: oxidase activity
Products: -
?
L-arginine + O2
4-guanidinobutanamide + CO2 + H2O
Substrates: -
Products: -
?
L-arginine + O2
4-guanidinobutyramide + CO2 + H2O
L-arginine + phenazine methosulfate
2-keto-5-guanidinovalerate + NH3 + reduced phenazine methosulfate
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Substrates: anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
Products: -
?
L-homoarginine + O2
?
-
Substrates: -
Products: -
?
L-lysine + electron acceptor
?
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Substrates: anaerobic conditions, electron acceptors are methylene blue, toluylene blue, phenol blue or thymol indophenol
Products: -
?
L-lysine + O2
2-keto-6-amino-n-hexanoate + NH3 + H2O2
-
Substrates: oxidase activity
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
L-lysine + O2
5-aminovaleramide + CO2 + H2O
L-Lysine + O2
?
-
Substrates: L-lysine degradation
Products: -
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L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
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Substrates: enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
Products: -
?
L-lysine + phenazine methosulfate
2-keto-6-amino-n-hexanoate + NH3 + reduced phenazine methosulfate
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Substrates: anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
Products: -
?
L-ornithine + O2
2-keto-5-amino-n-pentanoate + NH3 + H2O2
-
Substrates: oxidase activity
Products: -
?
L-ornithine + O2
4-aminobutanamide + CO2 + H2O
L-ornithine + O2 + H2O
5-amino-2-oxopentanoate + NH3 + H2O2
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Substrates: enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
Products: -
?
L-ornithine + phenazine methosulfate
2-keto-5-aminopentanoate + NH3 + reduced phenazine methosulfate
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Substrates: anaerobic conditions, ferricyanide as terminal electron acceptor, dehydrogenase activity
Products: -
?
L-thialysine + O2
?
-
Substrates: monooxygenase and oxidase activity
Products: -
?
Nepsilon-methyllysine + O2
5-methylaminopentanamide + CO2 + H2O
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Substrates: monooxygenase activity
Products: -
?
threo-4-hydroxy-L-lysine + O2
?
-
Substrates: oxidase activity
Products: -
?
additional information
?
-
L-arginine + O2
4-guanidinobutyramide + CO2 + H2O
-
Substrates: -
Products: -
?
L-arginine + O2
4-guanidinobutyramide + CO2 + H2O
-
Substrates: monooxygenase activity
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
Substrates: monooxygenase activity
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
Substrates: -
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
Substrates: -
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
Substrates: -
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
Substrates: -
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
Substrates: the mechanistic features are reported that are important for allowing the single active site of L-LOX/MOG to catalyze the two reactions of apparent monooxygenation and the oxidation of the flavoprotein oxidase
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
Substrates: -
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
Substrates: preferred substrate
Products: -
?
L-lysine + O2
5-aminopentanamide + CO2 + H2O
-
Substrates: enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
Products: -
?
L-lysine + O2
5-aminovaleramide + CO2 + H2O
-
Substrates: -
Products: -
?
L-lysine + O2
5-aminovaleramide + CO2 + H2O
-
Substrates: -
Products: -
?
L-ornithine + O2
4-aminobutanamide + CO2 + H2O
Substrates: -
Products: -
?
L-ornithine + O2
4-aminobutanamide + CO2 + H2O
-
Substrates: enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
Products: -
?
additional information
?
-
-
Substrates: analogs with a modified carboxyl or alpha-amino group are inactive as substrates
Products: -
?
additional information
?
-
-
Substrates: alkylamine dependent oxidation
Products: -
?
additional information
?
-
-
Substrates: alkylamine dependent oxidation
Products: -
?
additional information
?
-
-
Substrates: monooxygenase, oxidase and dehydrogenase reaction catalyzed by a single enzyme molecule
Products: -
?
additional information
?
-
-
Substrates: monooxygenase, oxidase and dehydrogenase reaction catalyzed by a single enzyme molecule
Products: -
?
additional information
?
-
-
Substrates: enzyme specific for O2 as electron acceptor, no dehydrogenase activity
Products: -
?
additional information
?
-
-
Substrates: alkylamine dependent oxygenation of alpha-monoamino acids
Products: -
?
additional information
?
-
-
Substrates: alkylamine dependent oxygenation of alpha-monoamino acids
Products: -
?
additional information
?
-
-
Substrates: L-lysine analogs with a chloro or hydroxyl group at either the delta or the gamma position are both oxygenated and oxidized
Products: -
?
additional information
?
-
Substrates: bifunctional L-amino acid oxidase, EC 1.4.3.2, of Pseudomonas sp. AIU813, renamed as L-amino acid oxidase/monooxygenase (L-AAO/MOG), exhibits L-lysine 2-monooxygenase as well as oxidase activity
Products: -
?
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C254A
site-directed mutagenesis, the mutant shows unaltered lysine 2-monooxygenase activity compared to the wild-type
C254D
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254E
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254F
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254G
site-directed mutagenesis, the mutant shows slightly reduced lysine 2-monooxygenase activity compared to the wild-type
C254H
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254I
site-directed mutagenesis, the mutant enzyme shows 5times higher specific activity of oxidase activity compared to wild-type, while the lysine 2-monooxygenase activity is completely abolished
C254M
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254N
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254P
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254Q
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254R
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254S
site-directed mutagenesis, the mutant shows slightly reduced lysine 2-monooxygenase activity compared to the wild-type
C254T
site-directed mutagenesis, the mutant shows unaltered lysine 2-monooxygenase activity compared to the wild-type
C254V
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254Y
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
D238A
the interaction of Asp238 with the terminal, positively charged group of the substrates is critical for substrate binding but not for catalytic control between the oxidase/monooxygenase activities
D238E
mutant displays increased catalytic activities
D238F
mutant exhibits altered substrate specificity to long hydrophobic substrates
C254L
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254L
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
C254W
site-directed mutagenesis, the mutant shows highly reduced lysine 2-monooxygenase activity compared to the wild-type
C254W
site-directed mutagenesis, the mutant shows moderately reduced lysine 2-monooxygenase activity compared to the wild-type
additional information
-
engineering of a recombinant Escherichia coli strain expressing the davB and davA genes for bioconversion of L-lysine to 5-aminovaleric acid resulting in low levels of 5-aminovalerate. Development of metabolically engineered Corynebacterium glutamicum strains for enhanced fermentative production of 5-aminovalerate from glucose. Expression of the Corynebacterium glutamicum codon-optimized davA gene fused with His6-Tag at its N-terminus and the davB gene as an operon under a strong synthetic H36 promoter (plasmid p36davAB3) in Corynebacterium glutamicum strain BE (pJS38) enables the most efficient production of 5-aminovalerate. The construct containing the His6-tagged variant produces substantially more 5-aminovalerate compared to that produced using the construct lacking the His-tag, possibly because of the improved stability afforded by the 5'-modification, which results in higher expression of the davAB genes in the recombinant Corynebacterium glutamicum BE strain. Deletion of the gabT gene (EC 2.6.1.19), encoding 4-aminobutyrate aminotransferase, improves the 5-aminovalerate production
additional information
Escherichia coli is engineered for production of 5-aminovalerate from L-lysine by coupled reaction of recombinant DavB, L-lysine monooxygenase, and recombinant DavA, 5-aminovaleramidase, overview. Under optimal conditions, 20.8 g/l 5-aminovalerate is produced from 30 g/l L-lysine in 12 h. Hydrogen peroxide, which is produced during the process of L-lysine oxidization, will further oxidize 6-amino-2-ketocaproic acid to form 5-aminovalerate as the final product. Method optimization, overview
additional information
-
Escherichia coli is engineered for production of 5-aminovalerate from L-lysine by coupled reaction of recombinant DavB, L-lysine monooxygenase, and recombinant DavA, 5-aminovaleramidase, overview. Under optimal conditions, 20.8 g/l 5-aminovalerate is produced from 30 g/l L-lysine in 12 h. Hydrogen peroxide, which is produced during the process of L-lysine oxidization, will further oxidize 6-amino-2-ketocaproic acid to form 5-aminovalerate as the final product. Method optimization, overview
additional information
-
Escherichia coli strain WL3110, coexpressing genes davB and davA, is used as whole-cell-catalyst for production of 5-aminovalerate from L-lysine, method optimization, overview
additional information
generation of an optimized production system for 5-aminovalerate from L-lysine in Escherichia coli by overexpressing genes davA and davB, encoding 5-aminovaleramide amidohydrolase and L-lysine 2-monooxygenase, the effects of induction conditions, reaction temperature, metal ion additives, and cell permeability on the whole-cell biocatalyst system are evaluated to improve biocatalytic efficiency, overview. Presence of Mn2+ and Ca2+ enhances the activity of whole-cell BL-22A-RB-YB system. Increased permeabilization of Escherichia coli BL-22A-RB-YB cells following surfactant treatment with TritonX-100 results in improved L-lysine consumption and 5-aminovalerate synthesis rate
additional information
-
installation of an expression system for production of 5-aminovalerate in Corynebacterium glutamicum strain LYS-12 by coexpressing gene davA, encoding 5-aminovaleramidase, and davB, encoding lysine monooxygenase, resulting in strains AVA-1-3. 5-Aminovalerate production is established. Related to the presence of endogenous genes coding for 5-aminovalerate transaminase (gabT) and glutarate semialdehyde dehydrogenase, 5-aminovalerate is partially converted to glutarate. Residual L-lysine is secreted as by-product. Putative gabT gene is deleted to enhance 5-aminovalerate production, method optimization and evaluation, overview
additional information
-
recombinant expression of gene davB in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase, lysine specific permease LysP, and PP2911, a 4-aminobutyrate transporter, since Escherichia coli is unable to assimilate L-lysine and to secrete 5-aminovalerate, reconstitution of Pseudomonas putida 5-aminovalerate pathway for production of 5-aminovalerate from L-lysine in Escherichia coli, biocatalysis conditions and method optimization, overview. Optimal temperature is 30°C
additional information
recombinant expression of gene davB in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase, lysine specific permease LysP, and PP2911, a 4-aminobutyrate transporter, since Escherichia coli is unable to assimilate L-lysine and to secrete 5-aminovalerate, reconstitution of Pseudomonas putida 5-aminovalerate pathway for production of 5-aminovalerate from L-lysine in Escherichia coli, biocatalysis conditions and method optimization, overview. Optimal temperature is 30°C
additional information
-
engineering of a recombinant Escherichia coli strain expressing the davB and davA genes for bioconversion of L-lysine to 5-aminovaleric acid resulting in low levels of 5-aminovalerate. Development of metabolically engineered Corynebacterium glutamicum strains for enhanced fermentative production of 5-aminovalerate from glucose. Expression of the Corynebacterium glutamicum codon-optimized davA gene fused with His6-Tag at its N-terminus and the davB gene as an operon under a strong synthetic H36 promoter (plasmid p36davAB3) in Corynebacterium glutamicum strain BE (pJS38) enables the most efficient production of 5-aminovalerate. The construct containing the His6-tagged variant produces substantially more 5-aminovalerate compared to that produced using the construct lacking the His-tag, possibly because of the improved stability afforded by the 5'-modification, which results in higher expression of the davAB genes in the recombinant Corynebacterium glutamicum BE strain. Deletion of the gabT gene (EC 2.6.1.19), encoding 4-aminobutyrate aminotransferase, improves the 5-aminovalerate production
-
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2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are coexpressed in Escherichia coli BL21(DE3) to produce nylon-5 monomer 5-aminovalerate from L-lysine
gene davB, recombinant expression in Corynebacterium glutamicum strain LYS-12, coexpression with Pseudomonas putida gene davA, encoding 5-aminovaleramidase
-
gene davB, recombinant expression in Escherichia coli strain WL3110, coexpression with gene davA, encoding 5-aminovaleramidase
-
gene davB, recombinant expression in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase, lysine specific permease LysP, and PP2911, a 4-aminobutyrate transporter, since Escherichia coli is unable to assimilate L-lysine and to secrete 5-aminovalerate
gene davB, recombinant expression in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase, recombinant expression of gene davB as N-terminally His-tagged enzyme in Corynebacterium glutamicum, a highly L-lysine producing strain BE using the sod promoter and the transcription factor Tu, EC 3.6.5.3
-
gene davB, recombinant expression of codon-optimized enzyme DavB in Escherichia coli strains BL21(DE3) and BL-22A-RB-YB, coexpression with gene davA, encoding 5-aminovaleramide amidohydrolase
gene davB, recombinant expression of His-tagged enzyme DavB in Escherichia coli, coexpression with gene davA, encoding 5-aminovaleramidase
gene laao/mog, recombinant expression of His-tagged wild-type enzyme L-amino acid oxidase/monooxygenase in Escherichia coli strain BL21(DE3), selenomethionine-labeled enzyme is expressed in Escherichia coli strain BL21 CodonPlus (DE3)-RIL-X
recombinantly expressed in Escherichia coli. Wild-type Escherichia coli enzyme can not convert lysine to 5-aminovalerate, whereas recombinant Escherichia coli enzyme expressing the davBA genes encoding lysine 2-monooxygenase and delta-aminovaleramidase produces 5-aminovalerate from lysine with a 64% conversion yield
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Flashner, M.S.; Massey, V.
Flavoprotein oxygenases
Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York
245-283
1974
Pseudomonas fluorescens
-
brenda
Karyakin, A.A.; Strakhova, A.K.; Karyakina, E.E.; Varfolomeev, S.D.; Simonyan, A.L.
Kinetic properties of L-lysine-2-monooxygenase from Pseudomonas putida and its application to biosensors for L-lysine
Prikl. Biokhim. Mikrobiol.
27
825-832
1991
Pseudomonas putida
-
brenda
Simonyan, A.L.; Khachatryan, G.E.; Tatikyan, S.S.; Avakyan, T.M.; Badalyan, I.E.
A flow-through enzyme analyzer for determination of L-lysine concentration
Biosens. Bioelectron.
6
93-99
1991
Pseudomonas putida
-
brenda
Ohnishi, T.; Yamamoto, S.; Hayaishi, O.; Izumi, T.; Shiba, T.
Studies on the reaction specificity of the flavoprotein lysine monooxygenase with modified substrates
Arch. Biochem. Biophys.
176
358-365
1976
Pseudomonas fluorescens
brenda
Maruyama, K.; Yamauchi, T.; Yamamoto, S.; Hayaishi, O.
A dehydrogenase reaction catalyzed by lysine monooxygenase, a flavooxygenase
Arch. Biochem. Biophys.
173
480-489
1976
Pseudomonas fluorescens
brenda
Yamauchi, T.; Yamamoto, S.; Hayaishi, O.
A possible involvement of sulfhydryl groups in the conversion of lysine monooxygenase to an oxidase
J. Biol. Chem.
250
7127-7133
1975
Pseudomonas fluorescens
brenda
Yamamoto, S.; Yamauchi, T.; Ohnishi, T.; Maruyama, K.; Hayaishi, O.
Alkylamine-dependent oxidation and oxygenation of alpha-monoamino acids by lysine monooxygenase
Arch. Biochem. Biophys.
171
316-326
1975
Pseudomonas fluorescens
brenda
Flashner, M.S.; Massey, V.
Regulatory properties of the flavoprotein L-lysine monooxygenase
J. Biol. Chem.
249
2587-2592
1974
Pseudomonas fluorescens
brenda
Flashner, M.I.S.; Massey, V.
Purification and properties of L-lysine monooxygenase from Pseudomonas fluorescens
J. Biol. Chem.
249
2579-2586
1974
Pseudomonas fluorescens
brenda
Yamauchi, T.; Yamamoto, S.; Hayaishi, O.
Reversible conversion of lysine monooxygenase to an oxidase by modification of sulfhydryl groups
J. Biol. Chem.
248
3750-3752
1973
Pseudomonas fluorescens
brenda
Yamamoto, S.; Yamauchi, T.; Hayaishi, O.
Alkylamine-dependent amino-acid oxidation by lysine monooxygenase--fragmented substrate of oxygenase
Proc. Natl. Acad. Sci. USA
69
3723-3726
1972
Pseudomonas fluorescens
brenda
Vandecasteele, J.P.; Hermann, M.
Regulation of a catabolic pathway. Lysine degradation in Pseudomonas putida
Eur. J. Biochem.
31
80-85
1972
Pseudomonas putida
brenda
Nakazawa, T.; Hori, K.; Hayaishi, O.
Studies on monooxygenases. V. Manifestation of amino acid oxidase activity by L-lysine monooxygenase
J. Biol. Chem.
247
3439-3444
1972
Pseudomonas fluorescens
brenda
Yamamoto, S.; Nakazawa, T.; Hayaishi, O.
Studies on monooxygenases. IV. Anaerobic formation of an alpha-keto acid by L-lysine monooxygenase
J. Biol. Chem.
247
3434-3438
1972
Pseudomonas fluorescens
brenda
Nakazawa, T.
Lysine oxygenase (Pseudomonas)
Methods Enzymol.
17B
154-157
1971
Pseudomonas fluorescens
-
brenda
Yamamoto, S.; Takeda, H.; Maki, Y.; Hayaishi, O.
Studies on monooxygenases. III. Examinations of metal participation in flavoprotein monooxygenases of pseudomonads
J. Biol. Chem.
244
2951-2955
1969
Pseudomonas fluorescens
brenda
Takeda, H.; Yamamoto, S.; Kojima, Y.; Hayaishi, O.
Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase
J. Biol. Chem.
244
2935-2941
1969
Pseudomonas fluorescens
brenda
Takeda, H.; Hayaishi, O.
Crystalline L-lysine oxygenase
J. Biol. Chem.
241
2733-2736
1966
Pseudomonas fluorescens
brenda
Park, S.J.; Kim, E.Y.; Noh, W.; Park, H.M.; Oh, Y.H.; Lee, S.H.; Song, B.K.; Jegal, J.; Lee, S.Y.
Metabolic engineering of Escherichia coli for the production of 5-aminovalerate and glutarate as C5 platform chemicals
Metab. Eng.
16
42-47
2013
Pseudomonas putida
brenda
Matsui, D.; Im, D.H.; Sugawara, A.; Fukuta, Y.; Fushinobu, S.; Isobe, K.; Asano, Y.
Mutational and crystallographic analysis of L-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 Interconversion between oxidase and monooxygenase activities
FEBS Open Bio
4
220-228
2014
Pseudomonas sp. AIU 813 (W6JQJ6)
brenda
Park, S.J.; Oh, Y.H.; Noh, W.; Kim, H.Y.; Shin, J.H.; Lee, E.G.; Lee, S.; David, Y.; Baylon, M.G.; Song, B.K.; Jegal, J.; Lee, S.Y.; Lee, S.H.
High-level conversion of L-lysine into 5-aminovalerate that can be used for nylon 6,5 synthesis
Biotechnol. J.
9
1322-1328
2014
Pseudomonas putida
brenda
Wang, X.; Cai, P.; Chen, K.; Ouyang, P.
Efficient production of 5-aminovalerate from L-lysine by engineered Escherichia coli whole-cell biocatalysts
J. Mol. Catal. B
134
115-121
2016
Pseudomonas putida (Q88QV1)
-
brenda
Rohles, C.; Giesselmann, G.; Kohlstedt, M.; Wittmann, C.; Becker, J.
Systems metabolic engineering of Corynebacterium glutamicum for the production of the carbon-5 platform chemicals 5-aminovalerate and glutarate
Microb. Cell Fact.
15
154
2016
Pseudomonas putida
brenda
Shin, J.H.; Park, S.H.; Oh, Y.H.; Choi, J.W.; Lee, M.H.; Cho, J.S.; Jeong, K.J.; Joo, J.C.; Yu, J.; Park, S.J.; Lee, S.Y.
Metabolic engineering of Corynebacterium glutamicum for enhanced production of 5-aminovaleric acid
Microb. Cell Fact.
15
174
2016
Pseudomonas putida, Pseudomonas putida ATCC 12633
brenda
Liu, P.; Zhang, H.; Lv, M.; Hu, M.; Li, Z.; Gao, C.; Xu, P.; Ma, C.
Enzymatic production of 5-aminovalerate from L-lysine using L-lysine monooxygenase and 5-aminovaleramide amidohydrolase
Sci. Rep.
4
5657
2014
Pseudomonas putida (Q88QV1), Pseudomonas putida
brenda
Li, Z.; Xu, J.; Jiang, T.; Ge, Y.; Liu, P.; Zhang, M.; Su, Z.; Gao, C.; Ma, C.; Xu, P.
Overexpression of transport proteins improves the production of 5-aminovalerate from L-lysine in Escherichia coli
Sci. Rep.
6
30884
2016
Pseudomonas putida, Pseudomonas putida (Q88QV1)
brenda
Im, D.; Matsui, D.; Arakawa, T.; Isobe, K.; Asano, Y.; Fushinobu, S.
Ligand complex structures of L-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 and its conformational change
FEBS open bio
8
314-324
2018
Pseudomonas sp. AIU 813 (W6JQJ6)
brenda
Trisrivirat, D.; Lawan, N.; Chenprakhon, P.; Matsui, D.; Asano, Y.; Chaiyen, P.
Mechanistic insights into the dual activities of the single active site of L-lysine oxidase/monooxygenase from Pseudomonas sp. AIU 813
J. Biol. Chem.
295
11246-11261
2020
Pseudomonas sp. (W6JQJ6), Pseudomonas sp. AIU 813
brenda